ArticleCell death and differentiation2026
Akt-mediated RALY phosphorylation functions as a molecular switch governing c-Myc stability.
Article in Cell death and differentiation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
10 authors.
Funding
Abstract
The oncoprotein c-Myc is frequently dysregulated in human cancers, yet the underlying mechanisms remain elusive. Here, we identify the RNA-binding protein RALY as a critical post-translational stabilizer of c-Myc. RALY homodimerizes and acts as a scaffold to bridge the deubiquitinating enzyme USP22 to c-Myc, thereby preventing c-Myc ubiquitination and proteasomal degradation. Under physiological growth factor stimulation, RALY is phosphorylated by Akt at S106 and T160. This phosphorylation event enables ternary complex formation with USP22 and c-Myc, promoting c-Myc stabilization and driving RALY's oncogenic activity. Furthermore, a synthetic peptide derived from RALY, termed RAMi, disrupts the RALY-USP22-c-Myc complex, destabilizes c-Myc, and exhibits potent anti-tumor effects. Together, these findings reveal Akt-mediated RALY phosphorylation as a molecular switch governing c-Myc stability and underscore the therapeutic potential of targeting the RALY-USP22-c-Myc axis in cancer.
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Registered trials
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